Evidence map›Paper›PMID 8991096›Full record

ArticleThe Journal of cell biology1996

The sup-pf-2 mutations of Chlamydomonas alter the activity of the outer dynein arms by modification of the gamma-dynein heavy chain.

G Rupp, E O'Toole, L C Gardner, B F Mitchell, M E Porter

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 82 citations in OpenAlex.

  1. Review
  2. PCD Genes-From Patients to Model Organisms and Back to Humans.International journal of molecular sciences · 2022
    Review
  3. A novel hypomorphic allele ofDisease models & mechanisms · 2020
    Article
  4. Asymmetries in the cilia ofPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    Review
  5. Article
  6. Article
  7. Article
  8. Ciliary Motility: Regulation of Axonemal Dynein Motors.Cold Spring Harbor perspectives in biology · 2017
    Review
  9. Review
  10. Article
  11. Article
  12. Alcohol-induced ciliary dysfunction targets the outer dynein arm.American journal of physiology. Lung cellular and molecular physiology · 2015
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

G RuppDepartment of Cell Biology and Neuroanatomy, University of Minnesota Medical School, Minneapolis 55455, USA.
E O'Toole
L C Gardner
B F Mitchell
M E Porter
University of Minnesota Medical Center · US

Funding

MOLECULAR STRATEGIES TO STUDY DYNEINF32GM017902 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI RUPP, GERALD · 1995 to 1997
–
NCRR NIH HHS RR00952NIGMS NIH HHS F32-GM17902
6 · The paper itself

Abstract

The sup-pf-2 mutation is a member of a group of dynein regulatory mutations that are capable of restoring motility to paralyzed central pair or radial spoke defective strains. Previous work has shown that the flagellar beat frequency is reduced in sup-pf-2, but little else was known about the sup-pf-2 phenotype (Huang, B., Z. Ramanis, and D.J.L. Luck. 1982. Cell. 28:115-125; Brokaw, C.J., and D.J.L. Luck. 1985. Cell Motil. 5:195-208). We have reexamined sup-pf-2 using improved biochemical and structural techniques and by the analysis of additional sup-pf-2 alleles. We have found that the sup-pf-2 mutations are associated with defects in the outer dynein arms. Biochemical analysis of sup-pf-2-1 axonemes indicates that both axonemal ATPase activity and outer arm polypeptides are reduced by 40-50% when compared with wild type. By thin-section EM, these defects correlate with an approximately 45% loss of outer dynein arm structures. Interestingly, this loss is biased toward a subset of outer doublets, resulting in a radial asymmetry that may reflect some aspect of outer arm assembly. The defects in outer arm assembly do not appear to result from defects in either the outer doublet microtubules or the outer arm docking structures, but rather appear to result from defects in outer dynein arm components. Analysis of new sup-pf-2 mutations indicates that the severity of the outer arm assembly defects varies with different alleles. Complementation tests and linkage analysis reveal that the sup-pf-2 mutations are alleles of the PF28/ODA2 locus, which is thought to encode the gamma-dynein heavy chain subunit of the outer arm. The sup-pf-2 mutations therefore appear to alter the activity of the outer dynein arms by modification of the gamma-dynein heavy chain.

Indexed as

AllelesAnimalsCell MovementChlamydomonasChromatography, Ion ExchangeDNA, ProtozoanDyneinsFlagellaGenetic Complementation TestImage Processing, Computer-AssistedIsomerismMicroscopy, ElectronMutationProtein Structure, TertiaryDNA, ProtozoanDyneins

Identifiers

PMID8991096
PMCPMC2133962
OpenAlexW2091432967

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.